disrupting the acyl carrier proteinspot interaction in vivo identification of acp residues involved in the interaction and consequence on growth扰乱体内酰基载体proteinspot交互识别acp残留参与互动和对经济增长的结果.pdfVIP

Disrupting the Acyl Carrier Protein/SpoT Interaction In Vivo: Identification of ACP Residues Involved in the Interaction and Consequence on Growth Sandra Angelini, Laetitia My, Emmanuelle Bouveret* Laboratory of Macromolecular System Engineering (LISM), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille University, Marseille, France Abstract In bacteria, Acyl Carrier Protein (ACP) is the central cofactor for fatty acid biosynthesis. It carries the acyl chain in elongation and must therefore interact successively with all the enzymes of this pathway. Yet, ACP also interacts with proteins of diverse unrelated function. Among them, the interaction with SpoT has been proposed to be involved in regulating ppGpp levels in the cell in response to fatty acid synthesis inhibition. In order to better understand this mechanism, we screened for ACP mutants unable to interact with SpoT in vivo by bacterial two-hybrid, but still functional for fatty acid synthesis. The position of the selected mutations indicated that the helix II of ACP is responsible for the interaction with SpoT. This suggested a mechanism of recognition similar to one used for the enzymes of fatty acid synthesis. Consistently, the interactions tested by bacterial two-hybrid of ACP with fatty acid synthesis enzymes were also affected by the mutations that prevented the interaction with SpoT. Yet, interestingly, the corresponding mutant strains were viable, and the phenotypes of one mutant suggested a defect in growth regulation. Citation: Angelini S, My L, Bouveret E (2012) Disrupting the Acyl Carrier Protein/SpoT Interaction In Vivo: Identification of ACP Residues Involved in the Interaction and Consequence on Growth. PLoS ONE 7(4): e36111. doi:10.1371/journal.pone.0036111 Editor: Anil Kumar Tyagi, University of Delhi, In